The Scribble polarity protein stabilizes E-cadherin/p120-catenin binding and blocks retrieval of E-cadherin to the Golgi
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Several polarity proteins, including Scribble (Scrb) have been implicated in control of vesicle traffic, and in particular the endocytosis of E-cadherin, but through unknown mechanisms. We now show that depletion of Scrb enhances endocytosis of E-cadherin by weakening the E-cadherin-p120catenin interaction. Unexpectedly, however, the internalized E-cadherin is not degraded but accumulates in the Golgi apparatus. Silencing p120-catenin causes degradation of E-cadherin in lysosomes, but degradation is blocked by the co-depletion of Scrb, which diverts the internalized E-cadherin to the Golgi. Loss of Scrb also enhances E-cadherin binding to retromer components, and retromer is required for Golgi accumulation of Scrb, and E-cadherin stability. These data identify a novel and unanticipated function for Scrb in blocking retromer-mediated diversion of E-cadherin to the Golgi. They provide evidence that polarity proteins can modify the intracellular itinerary for endocytosed membrane proteins.
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A more complete Scribble depletion revealed a role for Scribble in Ecad retention at the cell cortex, suggesting it stabilizes p120catenin-Ecad coupling, thus preventing retromer from diverting Ecad to the Golgi.
“A more complete Scribble depletion revealed a role for Scribble in Ecad retention at the cell cortex, suggesting it stabilizes p120catenin–Ecad coupling (Fig. 3 B; Lohia et al., 2012), thus preventing retromer from diverting Ecad to the Golgi.”
From Scribble: A master scaffold in polarity, adhesion, synaptogenesis, and proliferation (2019) · cites this paper as Lohia et al., 2012
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Awina, H. (2019) · theses.fr (ABES) · doi:10.70675/7b0a762dzd645z4e23z9222z2abee196c637
Cancer Cell Polarity and Extrusion
Rosenblatt, J., & Tchoumakova, A. (2026) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-071124-123101
- Authors
- Lohia, M., Qin, Y., & Macara, I. G.
- Affiliations
- University of Virginia (US)
- Vanderbilt University Medical Center (US)
- Corresponding author
- Macara, Ian G.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-11-30
- Volume
- 7
- Issue
- 11
- Pages
- e51130
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3511384
- OpenAlex
- W2067464510
- Cited by
- 64
- References
- 41
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 6 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 4 · 2019: 7 · 2018: 4 · 2017: 6 · 2016: 7 · 2015: 7 · 2014: 9
- FWCI
- 2.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Health and Human Services (GM070902)
- National Institutes of Health
- National Institute of General Medical Sciences (GM 070902, R01GM070902)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- Scribble, E-cadherin, p120 catenin, cell polarity, endocytosis, Golgi apparatus, retromer, protein stability, lysosomal degradation, membrane protein trafficking, vesicle traffic
- MeSH terms
- Delta Catenin, Animals, Cell Nucleus, Endocytosis, Golgi Apparatus, Humans, Lysosomes, Membrane Proteins, Models, Biological, Protein Binding, Cadherins, Cell Polarity, Protein Transport, Vesicular Transport Proteins, Catenins, Protein Stability, Madin Darby Canine Kidney Cells
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